Abstract
The ING2 plant homeodomain (PHD) finger is recruited to the nucleosome through specific binding to histone H3 trimethylated at lysine 4 (H3K4me3). Here, we describe backbone and side chain assignments of the ING2 PHD finger, analyze its binding to the unmodified and modified histone and p53 peptides, and map the histone H3 and H3K4me3 binding sites based on chemical shift perturbation analysis.
Copyright (c) 2009 John Wiley & Sons, Ltd.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Animals
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Binding Sites
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Conserved Sequence
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Crystallography, X-Ray
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Histones / chemistry*
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Homeodomain Proteins / chemistry*
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Magnetic Resonance Spectroscopy
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Mice
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Models, Molecular
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Reference Standards
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Sensitivity and Specificity
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Tumor Suppressor Protein p53 / chemistry
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Tumor Suppressor Proteins / chemistry*
Substances
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Histones
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Homeodomain Proteins
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ING2 protein, mouse
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Tumor Suppressor Protein p53
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Tumor Suppressor Proteins